ID   EFNB1_CHICK             Reviewed;         334 AA.
AC   O73612;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Ephrin-B1;
DE   AltName: Full=CEK5 ligand;
DE            Short=CEK5-L;
DE   Flags: Precursor;
GN   Name=EFNB1;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9070326; DOI=10.1006/dbio.1996.8496;
RA   Holash J.A., Soans C., Chong L.D., Shao H., Dixit V.M., Pasquale E.B.;
RT   "Reciprocal expression of the Eph receptor Cek5 and its ligand(s) in the
RT   early retina.";
RL   Dev. Biol. 182:256-269(1997).
CC   -!- FUNCTION: Cell surface transmembrane ligand for Eph receptors, a family
CC       of receptor tyrosine kinases which are crucial for migration, repulsion
CC       and adhesion during neuronal, vascular and epithelial development.
CC       Binds promiscuously Eph receptors residing on adjacent cells, leading
CC       to contact-dependent bidirectional signaling into neighboring cells.
CC       The signaling pathway downstream of the receptor is referred to as
CC       forward signaling while the signaling pathway downstream of the ephrin
CC       ligand is referred to as reverse signaling (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Binds to the receptor tyrosine kinase EPHB2. Interacts with
CC       GRIP1 and GRIP2 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC   -!- PTM: Inducible phosphorylation of tyrosine residues in the cytoplasmic
CC       domain. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ephrin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00884}.
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DR   EMBL; U72394; AAC07986.1; -; mRNA.
DR   RefSeq; NP_990366.1; NM_205035.2.
DR   AlphaFoldDB; O73612; -.
DR   SMR; O73612; -.
DR   STRING; 9031.ENSGALP00000039891; -.
DR   iPTMnet; O73612; -.
DR   GeneID; 395896; -.
DR   KEGG; gga:395896; -.
DR   CTD; 1947; -.
DR   VEuPathDB; HostDB:geneid_395896; -.
DR   eggNOG; KOG3858; Eukaryota.
DR   InParanoid; O73612; -.
DR   OrthoDB; 903831at2759; -.
DR   PhylomeDB; O73612; -.
DR   PRO; PR:O73612; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046875; F:ephrin receptor binding; IEA:InterPro.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0048013; P:ephrin receptor signaling pathway; IEA:InterPro.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   CDD; cd10426; Ephrin-B_Ectodomain; 1.
DR   Gene3D; 2.60.40.420; -; 1.
DR   InterPro; IPR008972; Cupredoxin.
DR   InterPro; IPR031328; Ephrin.
DR   InterPro; IPR034255; Ephrin-B_Ecto.
DR   InterPro; IPR019765; Ephrin_CS.
DR   InterPro; IPR001799; Ephrin_RBD.
DR   PANTHER; PTHR11304; PTHR11304; 1.
DR   Pfam; PF00812; Ephrin; 1.
DR   PRINTS; PR01347; EPHRIN.
DR   SUPFAM; SSF49503; SSF49503; 1.
DR   PROSITE; PS01299; EPHRIN_RBD_1; 1.
DR   PROSITE; PS51551; EPHRIN_RBD_2; 1.
PE   2: Evidence at transcript level;
KW   Developmental protein; Differentiation; Disulfide bond; Glycoprotein;
KW   Membrane; Neurogenesis; Phosphoprotein; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..334
FT                   /note="Ephrin-B1"
FT                   /id="PRO_0000008390"
FT   TOPO_DOM        26..231
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        232..252
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        253..334
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          26..160
FT                   /note="Ephrin RBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00884"
FT   REGION          175..218
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           332..334
FT                   /note="PDZ-binding"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        175..191
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        204..218
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        135
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        60..97
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00884"
FT   DISULFID        85..149
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00884"
SQ   SEQUENCE   334 AA;  36859 MW;  48AF556E9ED56CD5 CRC64;
     MARPRGGRWL LGVLLALCRL AAPLAKSLEP VSWSAGNPKF MSGKGLVIYP EIGDKLDIIC
     PKAEPSKPYD YYKLYLVKKD QADACSTVMD PNVLVTCNRP EQEIRFTIKF QEFSPNYMGL
     EFKRQQDYFI TSTSNGTLDG LENREGGVCQ TRSMKIVMKV GQDPNAVIPE QLTTSRPSKE
     ADNTVKIVTQ SPRHKVPTVE EPGKPGSVNQ NGQETQGPSD GFLSSKVAVF AAIGAGCVIF
     ILIIIFLVVL LIKIRKRHRK HTQQRAAALS LSTLASPKCS GNAGSEPSDI IIPLRTTENN
     YCPHYEKVSG DYGHPVYIVQ EMPPQSPANI YYKV